View source for 4wdi


==Weak TCR binding to an unstable insulin epitope drives type 1 diabetes==
<StructureSection load='4wdi' size='340' side='right'caption='[[4wdi]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wdi]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WDI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wdi OCA], [https://pdbe.org/4wdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wdi RCSB], [https://www.ebi.ac.uk/pdbsum/4wdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wdi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HA1D_MOUSE HA1D_MOUSE] Involved in the presentation of foreign antigens to the immune system.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The NOD mouse model of type 1 diabetes (T1D) continues to be an important tool for delineating the role of T-cell-mediated destruction of pancreatic beta-cells. However, little is known about the molecular mechanisms that enable this disease pathway. We show that insulin reactivity by a CD8+ T-cell clone known to induce T1D is characterised by weak T cell antigen receptor (TCR) binding to a relatively unstable peptide-major histocompatibility complex (pMHC). The structure of the native 9-mer and 10-mer insulin epitopes demonstrated that peptide residues 7 and 8 form a prominent solvent exposed bulge that could potentially be the main focus of TCR binding. The C-terminus of the peptide governed pMHC stability. Unexpectedly, we further demonstrate a novel mode of flexible peptide presentation in which the MHC peptide-binding groove is able to 'open the back door' to accommodate extra C-terminal peptide residues.

Distortion of the MHC class I binding groove to accommodate an insulin-derived 10-mer peptide.,Motozono C, Pearson JA, De Leenheer E, Rizkallah PJ, Beck K, Trimby A, Sewell AK, Wong FS, Cole DK J Biol Chem. 2015 Jun 17. pii: jbc.M114.622522. PMID:26085090<ref>PMID:26085090</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4wdi" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Cole DK]]
[[Category: Rizkallah PJ]]